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https://www.selleckchem.com/products/bay-985.html The ubiquitin-associated (UBA) domain is an important motif in the modulation of many molecular functionalities. It has been mainly associated with ubiquitin-mediated proteolysis, a multistep mechanism in which undesirable proteins are tagged with polyubiquitin chains for degradation in the proteasome complex. Comparison among UBA domains reveals a quite small structural variability, displaying an overall fold with a tightly packed three-helix bundle, and a common conserved hydrophobic patch on their surface that is important for ubiquitin binding. Mutations in the UBA domain, mainly in the highly conserved hydrophobic patch, induce conformational instabilities, which can be related to weak affinity for ubiquitin. This raises the question whether such hydrophobic patch presents conserved structural arrangement for selective recognition and protein binding. A concern that led us to investigate the stability of the p62-UBA domain as a case study regarding its structural arrangement as a function of temperature and two NaCl concentrations. Our results reveal that the temperature range and ionic strengths considered in this work produced a negligible effect on the three-helix bundle fold of p62-UBA domain.The interactions between tetrasulfophthalocyanines and lysozyme were studied using fluorescence spectroscopic and computational analyses. Lysozyme has been found to be widely studied as an anticancer agent, however, there are few reports of its interaction with phthalocyanines. Fe(III) tetrasulfophthalocyanine (FeTSPc) and free base tetrasulfophthalocyanine (TSPc) used in this study, were synthesized by our research group. Experimental results suggested that the metalled complex FeTSPc has a much higher affinity than TSPc. The binding stoichiometry between each tetrasulfophthalocyanine and lysozyme was 11. Stern-Volmer analysis suggested that the fluorescence quenching proceedes through a static process. Binding thermod

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